Anti-prion systems in yeast
| Autor: | Reed B. Wickner |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
0301 basic medicine
Saccharomyces cerevisiae Proteins Amyloid Prions animal diseases Saccharomyces cerevisiae Biochemistry Podospora anserina 03 medical and health sciences Amyloid disease mental disorders Humans Inositol phosphate Molecular Biology chemistry.chemical_classification Innate immune system 030102 biochemistry & molecular biology biology JBC Reviews Cell Biology biology.organism_classification Yeast nervous system diseases Cell biology 030104 developmental biology chemistry Chaperone (protein) biology.protein |
| Zdroj: | Journal of Biological Chemistry. 294:1729-1738 |
| ISSN: | 0021-9258 |
| DOI: | 10.1074/jbc.tm118.004168 |
| Popis: | Yeast prions have become important models for the study of the basic mechanisms underlying human amyloid diseases. Yeast prions are pathogenic (unlike the [Het-s] prion of Podospora anserina), and most are amyloid-based with the same in-register parallel β-sheet architecture as most of the disease-causing human amyloids studied. Normal yeast cells eliminate the large majority of prion variants arising, and several anti-prion/anti-amyloid systems that eliminate them have been identified. It is likely that mammalian cells also have anti-amyloid systems, which may be useful in the same way humoral, cellular, and innate immune systems are used to treat or prevent bacterial and viral infections. |
| Databáze: | OpenAIRE |
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